2014年8月8日 · The findings of strong nonpolar contacts between PKCα C1B and PMA, reduced contacts between the membrane and the C1B-PMA complex, and abnormally fast diffusion of the PMA-bound C1B domain may be relevant to the molecular mechanism of tumor promotion induced by PMA and other phorbol esters.

2004年11月13日 · Detailed molecular models of the free C1B domain of protein kinase C-γ (PKC-γ) and the C1B domain with its activator phorbol-12-myristate-13-acetate (PMA) in water solution and in the presence of dipalmitoylphosphatidylcholine (DPPC) bilayer are presented.

2018年5月1日 · In confocal experiments, deletion of the C1b domain from full length PKCθ diminished, whereas deletion of the C1a domain enhanced 5-fold (at 100 nM PMA) the translocation to the plasma membrane.

2009年1月9日 · Consistent with its potent sensitivity for PMA, the double δC1b (C1b-C1b/PKCδ-GFP) mutant also showed clear dose dependent down-regulation in response to PMA. These results suggest again that δC1b plays the major role in …

1999年7月30日 · Octyl-ILV thus resembles PMA in the difference in its C1 domain dependence between PKCα and PKCδ, shifting from dependence primarily on C1b in PKCδ to equivalence of C1a and C1b in PKCα. Our findings have several important implications.

2003年9月30日 · Novel and conventional protein kinase C isozymes contain a tandem repeat of C1 domains, the C1A and C1B, which each contain a binding pocket for phorbol esters/diacylglycerol. This study addresses the contribution of the C1A and C1B domains in the regulation of protein kinase C's membrane interaction using bisfunctional (dimeric) phorbol ...

Detailed molecular models of the free C1B domain of protein kinase C-γ (PKC-γ) and the C1B domain with its activator phorbol-12-myristate-13-acetate (PMA) in water solution and in the presence of dipalmitoylphosphatidylcholine (DPPC) bilayer are presented.

either the C1A or C1B domains are mutated so that they are unable to bind PMA, if one moiety of the dimer contains a nonfunctional phorbol, or if the binding to the isolated C1B domain is measured. Thus, the increased potency of the dimeric phorbol esters results primarily from their ability to engage, to a

2004年12月16日 · Detailed molecular models of the free C1B domain of protein kinase C-gamma (PKC-gamma) and the C1B domain with its activator phorbol-12-myristate-13-acetate (PMA) in water solution and in the presence of dipalmitoylphosphatidylcholine (DPPC) bilayer are …

We show that the cysteine-rich repeat C1b is responsible for its Golgi localization, while for its presence at the ER/nuclear envelope the pseudosubstrate containing fragment coupled to the C1 domain is required. In response to short-term activation by PMA we show translocation of PKCeta to the plasma membrane and the nuclear envelope.